D1.2-Protein-Synthesis
D1.2-Protein-Synthesis
❓ Distinguish between
the structures of RNA
and DNA.
RNA DNA
Number of Strands 1 2
Sugar Ribose Deoxyribose
Uracil Thymine
Adenine Adenine
Nitrogen Bases
Cytosine Cytosine
Guanine Guanine
RNA and DNA
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From
D1.2.1: Transcription as the synthesis of the IB
Transcription
Transcription is the
synthesis of RNA,
using DNA as a
template.
The enzyme RNA
polymerase
transcribes DNA to
RNA.
❓ Explain
transcription.
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Transcription
RNA polymerase attaches to the
beginning of a gene on DNA.
RNA polymerase separates the
DNA strands.
An mRNA molecule is produced on
the template DNA strand, using
the enzyme RNA polymerase to
link RNA nucleotides into a single
polynucleotide (by condensation
reactions). Transcription
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Transcription
RNA polymerase uses
complementary base pairing to
pair DNA and RNA nucleotides.
RNA polymerase reaches the end
of the gene, and the mRNA
molecule is released.
Transcription
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From
D1.2.2: Role of hydrogen bonding and the IB
Include the pairing of adenine (A) on the DNA template strand with
uracil (U) on the RNA strand.
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DNA and RNA Complementary Base Pairs
During transcription, RNA nucleotides form complementary base pairs
with DNA nucleotides of the gene being transcribed.
The DNA and RNA bases are held together by hydrogen bonds.
The DNA - RNA base pairs are:
DNA Base RNA Base
Adenine (A) Uracil (U)
Guanine (G) Cytosine (C)
Cytosine (C) Guanine (G)
Thymine (T) Adenine (A)
Note: Adenine bases in DNA pair with Uracil bases in RNA.
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From
D1.2.3: Stability of DNA templates the IB
Stability of DNA
DNA is a stable molecule, due to the strong
covalent bonds between the nucleotides.
Single DNA strands can be used as a
template for transcribing a base sequence,
without the DNA base sequence changing.
In somatic cells that do not divide, such
sequences must be conserved throughout
the life of a cell.
DNA is a stable molecule.
Somatic cells are non-reproductive cells in
an organism.
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From
D1.2.4: Transcription as a process required the IB
Protein Synthesis
The base sequence of mRNA is translated into the amino acid sequence
of a polypeptide.
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Translation
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From
D1.2.6: Roles of mRNA, ribosomes and the IB
tRNA in translation
Students should know that mRNA binds to the small subunit of the
ribosome and that two tRNAs can bind simultaneously to the large
subunit.
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Ribosomes
Ribosomes are organelles found in
cells which translate the genetic
code of mRNA to a polypeptide.
Ribosomes are composed of two
subunits:
● Small subunit
● Large subunit
Two tRNA molecules can bind
simultaneously to the large subunit
of a ribosome. Ribosome
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Messenger RNA
Messenger RNA (mRNA) contains the
genetic code in the form of codons.
mRNA binds to the small subunit of a
ribosome to initiate translation.
Codons are a sequence of three
nucleotides that code for an amino acid.
Ribosomes use the sequence of codons on
mRNA to determine the sequence of
amino acids in a polypeptide.
Codons are on mRNA
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Transfer RNA
Transfer RNA (tRNA) transfers amino acids Amino acid binding
site
from the cytoplasm to the ribosome.
tRNA molecules have an anticodon, which
binds to mRNA codons.
The binding of codons of mRNA and
anticodons of tRNA in the ribosome by
complementary base pairing ensures that Anticodon
The sequence of
amino acids in a
polypeptide can be
determined using
the codon
sequences in
mRNA, combined
with a table of
mRNA codons.
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Determine the Genetic Code
❓ Identify the amino acid for the
codon CUA.
The base sequence of mRNA is translated into the amino acid sequence
of a polypeptide.
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Movement of Ribosomes
The ribosome moves along mRNA from codon to codon.
At each codon, a tRNA enters the ribosome.
When two tRNAs are present in the ribosome, a peptide
bond forms between their amino acids.
One tRNA loses its amino acid, and leaves the ribosome.
The polypeptide chain grows as the ribosome moves from
codon to codon.
The polypeptide, small and large ribosomal subunits and
tRNA are released when a stop codon enters the ribosome.
Ribosomes move along mRNA
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Translation
Carefully review
all of the
information on
the previous
slides and watch
the video so
that you
understand
translation.
❓ Describe
translation.
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Translation
Translation is the synthesis of polypeptides using the
genetic code of mRNA by ribosomes.
There are specific codons for each amino acid on the
mRNA.
The small ribosomal subunit binds to mRNA at the start
codon.
A tRNA with a complementary anticodon binds to the
mRNA codon by hydrogen bonding.
The large ribosomal subunit attaches to form a ribosome.
Translation
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Translation
A second tRNA molecule enters the ribosome, as there
are two tRNA binding sites in the large ribosomal subunit.
A peptide bond forms between the two amino acids by a
condensation reaction, releasing one tRNA from the
ribosome.
The ribosome moves from codon to codon along the
mRNA, adding amino acids to a growing polypeptide.
When the ribosome reaches a stop codon, the large and
small subunits separate.
The tRNA and polypeptide are released.
Translation
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From
D1.2.11: Mutations that change protein the IB
structure
Mutations
A mutation is a
change to the DNA
sequence of an
organism.
A mutation to a
single nucleotide in
the gene for
haemoglobin can
cause the disease
sickle cell anaemia.
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Questions
https://www.youtube.com/watch?v=dFYBBFEKg6E
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translation
Students should understand what is meant by 5' to 3' transcription and
5' to 3' translation.
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Directionality of RNA
Transcription of mRNA
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promoter
Stages of Transcription
https://www.youtube.com/watch?v=6KYXxvG5zWs
Transcription
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eukaryotic cells
https://www.youtube.com/watch?v=DoSRu15VtdM
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❓ Explain how
mRNA is
processed to
remove the
introns.
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Splicing of Exons
Exons from one mRNA can be spliced together in different
combinations.
One gene may code for different proteins, based on how the exons are
spliced together.
Translation
Translation involves three
stages:
● Initiation
● Elongation
● Termination
HL students require more
detail than SL students if they
are asked to explain
translation
Translation
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Translation: Initiation
The small ribosomal subunit binds to the mRNA at the
start codon (AUG).
A tRNA molecule with the anticodon complementary to the
start codon binds to the mRNA .
The large ribosomal subunit binds to the small ribosomal
subunit.
The tRNA is in the P site. A second codon enters the A site.
A tRNA with the complementary anticodon
(complementary to the second codon) enters the A site.
A peptide bond forms between the two amino acids. Initiation of Translation
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Translation: Elongation
The elongation of the polypeptide
involves a repeated cycle of events:
● The ribosome moves (translocates)
along the mRNA by three bases
towards the 3’ end of the mRNA.
Moving one tRNA into the E site,
which exits the ribosome.
● A new tRNA is in the P site. A new
tRNA (with the anticodon
Elongation of Polypeptides
complementary to the codon) with
amino acid enters the A site.
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Translation: Elongation
● The two neighbouring amino acids
bond, resulting in a growing
polypeptide chain.
Elongation of Polypeptides
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Translation: Termination
A stop codon enters the A site, then:
● No tRNA is available to enter the A site, causing the release of the
polypeptide from the P site.
● The tRNA detaches from the ribosome.
● The mRNA detaches from the ribosome.
● The large subunit and small subunit separate.
The polypeptide may need to be modified after translation to become a
functional protein.
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From
D1.2.18: Modification of polypeptides into the IB
Modification of Polypeptides
Many Review the information below the linked image.
polypeptides
must be modified
after translation
before they can
function.
❓ Explain how
pre-proinsulin
is modified to
form insulin.
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Modification of Pre-Proinsulin
Pre-proinsulin is formed by transcription and
translation.
Pre-proinsulin is converted to functional insulin
in two steps:
Formation of Proinsulin:
A signal peptide is removed from preproinsulin
within the rough endoplasmic reticulum to form
proinsulin.
Modification of Pre-Proinsulin
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Modification of Pre-Proinsulin
Formation of Insulin:
Proinsulin is sent to the Golgi apparatus, and is
packaged into a secretory vesicle.
Within the secretory vesicle, a protein chain is
removed from proinsulin to form an alpha chain
and a beta chain.
The alpha and beta chains join by disulfide
bonds to form functional insulin.
Insulin is secreted into the bloodstream by
exocytosis. Modification of Pre-Proinsulin
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From
D1.2.19: Recycling of amino acids by the IB
proteasomes
Limit to the understanding that sustaining a functional proteome
requires constant protein breakdown and synthesis.
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Proteasomes
A proteome is the entire complement of proteins that is expressed by a
cell or organism.
The cell synthesizes all of the proteins required by the cell.
Proteins which are no longer required are broken down to amino acids
by proteasomes.
Proteasomes are large protein complexes which break down unneeded
proteins to amino acids through hydrolysis reactions.
The amino acids are recycled to synthesize proteins that are required by
the cell.
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Questions
Criterion A Resources
Final Exams 2024 - Current Course
Criteria B and C Resources
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